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HEADER SERINE CARBOXYPEPTIDASE 07-MAR-94 1WHT 1WHT 2
COMPND SERINE CARBOXYPEPTIDASE II (E.C.3.4.16.1) COMPLEXED WITH 1WHT 3
COMPND 2 L-BENZYLSUCCINATE 1WHT 4
SOURCE WHEAT (TRITICUM VULGARIS) GERM 1WHT 5
AUTHOR T.L.BULLOCK,S.J.REMINGTON 1WHT 6
REVDAT 1 22-JUN-94 1WHT 0 1WHT 7
JRNL AUTH T.L.BULLOCK,S.J.REMINGTON 1WHT 8
JRNL TITL STRUCTURE OF THE COMPLEX OF L-BENZYLSUCCINATE WITH 1WHT 9
JRNL TITL 2 WHEAT SERINE CARBOXYPEPTIDASE II AT 2.0 ANGSTROMS 1WHT 10
JRNL TITL 3 RESOLUTION 1WHT 11
JRNL REF TO BE PUBLISHED REF NOW ASSIGNED AS 1WHT 12
JRNL REFN 0353 1WHT 13
REMARK 1 1WHT 14
REMARK 1 REFERENCE 1 1WHT 15
REMARK 1 AUTH D.-I.LIAO,S.J.REMINGTON 1WHT 16
REMARK 1 TITL STRUCTURE OF WHEAT SERINE CARBOXYPEPTIDASE II AT 1WHT 17
REMARK 1 TITL 2 3.5 ANGSTROMS RESOLUTION 1WHT 18
REMARK 1 REF J.BIOL.CHEM. V. 265 6528 1990 1WHT 19
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 0071 1WHT 20
REMARK 1 REFERENCE 2 1WHT 21
REMARK 1 AUTH K.P.WILSON,D.-I.LIAO,T.BULLOCK,S.J.REMINGTON, 1WHT 22
REMARK 1 AUTH 2 K.BREDDAM 1WHT 23
REMARK 1 TITL CRYSTALLIZATION OF SERINE CARBOXYPEPTIDASES 1WHT 24
REMARK 1 REF J.MOL.BIOL. V. 211 301 1990 1WHT 25
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070 1WHT 26
REMARK 1 REFERENCE 3 1WHT 27
REMARK 1 AUTH K.BREDDAM,S.B.SORENSEN,I.SVENDSEN 1WHT 28
REMARK 1 TITL PRIMARY STRUCTURE AND ENZYMATIC PROPERTIES OF 1WHT 29
REMARK 1 TITL 2 CARBOXYPEPTIDASE II FROM WHEAT BRAN 1WHT 30
REMARK 1 REF CARLSBERG RES.COMMUN. V. 52 297 1987 1WHT 31
REMARK 1 REFN ASTM CRCODS DK ISSN 0105-1938 0915 1WHT 32
REMARK 2 1WHT 33
REMARK 2 RESOLUTION. 2.0 ANGSTROMS. 1WHT 34
REMARK 3 1WHT 35
REMARK 3 REFINEMENT. 1WHT 36
REMARK 3 PROGRAM TNT 1WHT 37
REMARK 3 AUTHORS TRONRUD,TEN EYCK,MATTHEWS 1WHT 38
REMARK 3 R VALUE 0.176 1WHT 39
REMARK 3 RMSD BOND DISTANCES 0.017 ANGSTROMS 1WHT 40
REMARK 3 RMSD BOND ANGLES 2.6 DEGREES 1WHT 41
REMARK 3 1WHT 42
REMARK 3 NUMBER OF PROTEIN ATOMS 3216 1WHT 43
REMARK 3 NUMBER OF SOLVENT ATOMS 430 1WHT 44
REMARK 3 1WHT 45
REMARK 3 RESTRAINED B-FACTORS: 3.8 ANGSTROMS**2. 1WHT 46
REMARK 4 1WHT 47
REMARK 4 THE L-BENZYLSUCCINATE COMPLEX WAS SOLVED AT -170 DEGREES 1WHT 48
REMARK 4 CELSIUS. 1WHT 49
REMARK 5 1WHT 50
REMARK 5 RESIDUES GLU 24, ARG 74, LYS 163 OF CHAIN *A* AND ARG 282, 1WHT 51
REMARK 5 AND GLN 375A OF CHAIN *B* HAVE INCOMPLETE SIDE CHAIN ATOMS. 1WHT 52
REMARK 6 1WHT 53
REMARK 6 PDB ADVISORY NOTICE: 1WHT 54
REMARK 6 THERE ARE A FEW WATER MOLECULES WHICH MAY BE ASSOCIATED 1WHT 55
REMARK 6 WITH SYMMETRY RELATED PROTEIN MOLECULES. 1WHT 56
SEQRES 1 A 256 GLY HIS ALA ALA ASP ARG ILE ALA ARG LEU PRO GLY GLN 1WHT 57
SEQRES 2 A 256 PRO ALA VAL ASP PHE ASP MET TYR SER GLY TYR ILE THR 1WHT 58
SEQRES 3 A 256 VAL ASP GLU GLY ALA GLY ARG SER LEU PHE TYR LEU LEU 1WHT 59
SEQRES 4 A 256 GLN GLU ALA PRO GLU ASP ALA GLN PRO ALA PRO LEU VAL 1WHT 60
SEQRES 5 A 256 LEU TRP LEU ASN GLY GLY PRO GLY CYS SER SER VAL ALA 1WHT 61
SEQRES 6 A 256 TYR GLY ALA SER GLU GLU LEU GLY ALA PHE ARG VAL LYS 1WHT 62
SEQRES 7 A 256 PRO ARG GLY ALA GLY LEU VAL LEU ASN GLU TYR ARG TRP 1WHT 63
SEQRES 8 A 256 ASN LYS VAL ALA ASN VAL LEU PHE LEU ASP SER PRO ALA 1WHT 64
SEQRES 9 A 256 GLY VAL GLY PHE SER TYR THR ASN THR SER SER ASP ILE 1WHT 65
SEQRES 10 A 256 TYR THR SER GLY ASP ASN ARG THR ALA HIS ASP SER TYR 1WHT 66
SEQRES 11 A 256 ALA PHE LEU ALA LYS TRP PHE GLU ARG PHE PRO HIS TYR 1WHT 67
SEQRES 12 A 256 LYS TYR ARG ASP PHE TYR ILE ALA GLY GLU SER TYR ALA 1WHT 68
SEQRES 13 A 256 GLY HIS TYR VAL PRO GLU LEU SER GLN LEU VAL HIS ARG 1WHT 69
SEQRES 14 A 256 SER LYS ASN PRO VAL ILE ASN LEU LYS GLY PHE MET VAL 1WHT 70
SEQRES 15 A 256 GLY ASN GLY LEU ILE ASP ASP TYR HIS ASP TYR VAL GLY 1WHT 71
SEQRES 16 A 256 THR PHE GLU PHE TRP TRP ASN HIS GLY ILE VAL SER ASP 1WHT 72
SEQRES 17 A 256 ASP THR TYR ARG ARG LEU LYS GLU ALA CYS LEU HIS ASP 1WHT 73
SEQRES 18 A 256 SER PHE ILE HIS PRO SER PRO ALA CYS ASP ALA ALA THR 1WHT 74
SEQRES 19 A 256 ASP VAL ALA THR ALA GLU GLN GLY ASN ILE ASP MET TYR 1WHT 75
SEQRES 20 A 256 SER LEU TYR THR PRO VAL CYS ASN ILE 1WHT 76
SEQRES 1 B 153 SER TYR ASP PRO CYS THR GLU ARG TYR SER THR ALA TYR 1WHT 77
SEQRES 2 B 153 TYR ASN ARG ARG ASP VAL GLN MET ALA LEU HIS ALA ASN 1WHT 78
SEQRES 3 B 153 VAL THR GLY ALA MET ASN TYR THR TRP ALA THR CYS SER 1WHT 79
SEQRES 4 B 153 ASP THR ILE ASN THR HIS TRP HIS ASP ALA PRO ARG SER 1WHT 80
SEQRES 5 B 153 MET LEU PRO ILE TYR ARG GLU LEU ILE ALA ALA GLY LEU 1WHT 81
SEQRES 6 B 153 ARG ILE TRP VAL PHE SER GLY ASP THR ASP ALA VAL VAL 1WHT 82
SEQRES 7 B 153 PRO LEU THR ALA THR ARG TYR SER ILE GLY ALA LEU GLY 1WHT 83
SEQRES 8 B 153 LEU PRO THR THR THR SER TRP TYR PRO TRP TYR ASP ASP 1WHT 84
SEQRES 9 B 153 GLN GLU VAL GLY GLY TRP SER GLN VAL TYR LYS GLY LEU 1WHT 85
SEQRES 10 B 153 THR LEU VAL SER VAL ARG GLY ALA GLY HIS GLU VAL PRO 1WHT 86
SEQRES 11 B 153 LEU HIS ARG PRO ARG GLN ALA LEU VAL LEU PHE GLN TYR 1WHT 87
SEQRES 12 B 153 PHE LEU GLN GLY LYS PRO MET PRO GLY GLN 1WHT 88
FTNOTE 1 1WHT 89
FTNOTE 1 CIS PROLINE - PRO A 43 1WHT 90
FTNOTE 2 1WHT 91
FTNOTE 2 CIS PROLINE - PRO A 54 1WHT 92
FTNOTE 3 1WHT 93
FTNOTE 3 CIS PROLINE - PRO A 96 1WHT 94
HET BZS 430 15 L-BENZYLSUCCINATE 1WHT 95
HET NAG 1131 14 N-ACETYL-D-GLUCOSAMINE 1WHT 96
HET FUC A 105A 10 FUCOSE 1WHT 97
HET NAG 1051 14 N-ACETYL-D-GLUCOSAMINE 1WHT 98
HET NAG 1052 14 N-ACETYL-D-GLUCOSAMINE 1WHT 99
HET NAG 2911 14 N-ACETYL-D-GLUCOSAMINE 1WHT 100
HET NAG 2912 14 N-ACETYL-D-GLUCOSAMINE 1WHT 101
FORMUL 3 BZS C11 H10 O4 1WHT 102
FORMUL 4 NAG 5(C8 H15 N1 O6) 1WHT 103
FORMUL 5 FUC C6 H12 O6 1WHT 104
FORMUL 6 HOH *430(H2 O1) 1WHT 105
HELIX 1 H1 PRO A 38 GLN A 42 5 1WHT 106
HELIX 2 H2 GLY A 61 GLU A 64 1 1WHT 107
HELIX 3 H3 ARG A 83 VAL A 87 5 1WHT 108
HELIX 4 H4 ASP A 112C ARG A 129 1 1WHT 109
HELIX 5 H5 ALA A 148 ARG A 161 1 1WHT 110
HELIX 6 H6 ASP A 181 ASN A 194 1 1WHT 111
HELIX 7 H7 ASP A 200 CYS A 210 1 1WHT 112
HELIX 8 H8 PRO A 220 GLN A 233 1 1WHT 113
HELIX 9 H9 THR B 271 TYR B 279 1 1WHT 114
HELIX 10 H10 SER B 282 LEU B 288 1 1WHT 115
HELIX 11 H11 ASP B 303B THR B 307 1 1WHT 116
HELIX 12 H12 LEU B 314 ILE B 321 1 1WHT 117
HELIX 13 H13 LEU B 343 GLY B 351 1 1WHT 118
HELIX 14 H14 VAL B 399 HIS B 402 1 1WHT 119
HELIX 15 H15 PRO B 404 GLN B 416 1 1WHT 120
SHEET 1 S1 11 ASP A -1 ILE A 1 0 1WHT 121
SHEET 2 S1 11 MET A 16 ASP A 23A-1 1WHT 122
SHEET 3 S1 11 ARG A 28 LEU A 34 -1 1WHT 123
SHEET 4 S1 11 ALA A 88 PHE A 92 -1 1WHT 124
SHEET 5 S1 11 LEU A 46 LEU A 50 1 1WHT 125
SHEET 6 S1 11 ASP A 139 GLU A 145 1 1WHT 126
SHEET 7 S1 11 ASN A 168 GLY A 175 1 1WHT 127
SHEET 8 S1 11 ARG B 329 GLY B 335 1 1WHT 128
SHEET 9 S1 11 LEU B 387 VAL B 392 1 1WHT 129
SHEET 10 S1 11 GLU B 376 TYR B 384 -1 1WHT 130
SHEET 11 S1 11 THR B 366 TYR B 373 -1 1WHT 131
SHEET 1 S2 2 PHE A 69 VAL A 71 0 1WHT 132
SHEET 2 S2 2 LEU A 77 LEU A 79 -1 1WHT 133
SHEET 1 S3 1 SER A 102 ASN A 105 0 1WHT 134
TURN 1 T01 LEU A 4 GLN A 7 1WHT 135
TURN 2 T02 LYS A 72 GLY A 75 1WHT 136
TURN 3 T03 ASN A 80 ARG A 83 1WHT 137
TURN 4 T04 PRO A 96 VAL A 99 1WHT 138
TURN 5 T05 VAL A 99 SER A 102 1WHT 139
TURN 6 T06 SER A 108 TYR A 111 1WHT 140
TURN 7 T07 PRO A 131 LYS A 134 1WHT 141
TURN 8 T08 TYR A 133 ARG A 138 1WHT 142
TURN 9 T09 ASN A 164 ILE A 167 1WHT 143
TURN 10 T10 CYS A 210 ASP A 213 1WHT 144
TURN 11 T11 ASP A 237 SER A 240 1WHT 145
TURN 12 T12 MET B 286 HIS B 289 1WHT 146
TURN 13 T13 ASN B 291 GLY B 294 1WHT 147
TURN 14 T14 GLY B 335 ASP B 338 1WHT 148
TURN 15 T15 ASP B 374 GLU B 376 1WHT 149
TURN 16 T16 TYR B 384 LEU B 387 1WHT 150
TURN 17 T17 VAL B 392 ALA B 395 1WHT 151
SSBOND 1 CYS A 56 CYS B 303 1WHT 152
SSBOND 2 CYS A 210 CYS A 222 1WHT 153
SSBOND 3 CYS A 246 CYS B 268 1WHT 154
SITE 1 ACT 4 ASP B 338 HIS B 397 SER A 146 GLU A 145 1WHT 155
CRYST1 95.500 95.500 208.600 90.00 90.00 90.00 P 41 21 2 8 1WHT 156
ORIGX1 1.000000 0.000000 0.000000 0.00000 1WHT 157
ORIGX2 0.000000 1.000000 0.000000 0.00000 1WHT 158
ORIGX3 0.000000 0.000000 1.000000 0.00000 1WHT 159
SCALE1 0.010471 0.000000 0.000000 0.00000 1WHT 160
SCALE2 0.000000 0.010471 0.000000 0.00000 1WHT 161
SCALE3 0.000000 0.000000 0.004794 0.00000 1WHT 162 |